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Information on EC 1.10.3.2 - laccase

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EC Tree
     1 Oxidoreductases
         1.10 Acting on diphenols and related substances as donors
             1.10.3 With oxygen as acceptor
                1.10.3.2 laccase
IUBMB Comments
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
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This record set is specific for:
UNIPROT: B0JDP9
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
laccase, lacc, phenol oxidase, laccase a, cota-laccase, lac i, diphenol oxidase, poxa1b, laccase2, cota laccase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Benzenediol:oxygen oxidoreductase
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Diphenol oxidase
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Laccase allele OR
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Laccase allele TS
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Ligninolytic phenoloxidase
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p-diphenol oxidase
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urishiol oxidase
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urushiol oxidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
benzenediol:oxygen oxidoreductase
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
CAS REGISTRY NUMBER
COMMENTARY hide
80498-15-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
show the reaction diagram
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-
?
4 2,6-dimethoxyphenol + O2
?
show the reaction diagram
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-
?
4 3,3',5,5'-tetramethylbenzidine + O2
?
show the reaction diagram
-
-
-
?
4 guaiacol + O2
?
show the reaction diagram
-
-
-
?
4 syringaldazine + O2
?
show the reaction diagram
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.058 - 3.703
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.26 - 100.7
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.074 - 6.434
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6.5
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ERY4
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B0JDP9_PLEER
533
0
58068
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K532A
site-directed mutagenesis, the mutant shows increased catalytic efficiency and altered substrate specificity compared to the wild-type enzyme
K532E
site-directed mutagenesis, the mutant shows increased catalytic efficiency and altered substrate specificity compared to the wild-type enzyme
K532R
site-directed mutagenesis, inactive mutant
P530A
site-directed mutagenesis, the mutant shows increased catalytic efficiency and altered substrate specificity compared to the wild-type enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Saccharomyces cerevisiae by anion exchange chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ery4 genetic structure, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bleve, G.; Lezzi, C.; Spagnolo, S.; Tasco, G.; Tufariello, M.; Casadio, R.; Mita, G.; Rampino, P.; Grieco, F.
Role of the C-terminus of Pleurotus eryngii Ery4 laccase in determining enzyme structure, catalytic properties and stability
Protein Eng. Des. Sel.
26
1-13
2013
Pleurotus eryngii (B0JDP9), Pleurotus eryngii
Manually annotated by BRENDA team